MolNFT v1 · #116453 · protein
Structural mechanism of NEK7 activation by NEK9-induced dimerisation
5DE2: “Structural mechanism of NEK7 activation by NEK9-induced dimerisation”. X-ray diffraction. MolNFT v1 #116453 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5DE2
- Type
- protein
- Length
- 554 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8TDX7, Q8K1R7
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 267 | — | Q8TDX7 |
| B | — | protein | 262 | — | Q8TDX7 |
| C | — | protein | 16 | — | Q8K1R7 |
| D | — | protein | 9 | — | Q8K1R7 |
Compared structures
- 5DE2 · Structural mechanism of Nek7 activation by Nek9-induced dimerisation · the same entry in another collection · chain D against D, TM-score 1.00
- Q8TDX7 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase NEK7 (Q8TDX7) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q8K1R7 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase NEK9 (Q8K1R7) · a predicted model of the same protein · chain D against A, TM-score 0.78
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8TDX7
- Every structure of UniProt Q8K1R7
- Elsewhere: RCSB PDB 5DE2 · PDBe 5DE2 · UniProt Q8TDX7 · UniProt Q8K1R7
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